Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01021286001 |
Family | CBM57 |
Protein Properties | Length: 1902 Molecular Weight: 218308 Isoelectric Point: 6.1165 |
Chromosome | Chromosome/Scaffold: 10 Start: 3464257 End: 3493620 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 1313 | 1494 | 1.5e-27 |
HINCGGGRTIIGDIVYEADEDLAGPSKFVPTRDNWGFSSTGDFWDRDRTTKNYIAHNVSMLGMNDSELYTRARLSPLSYTYYGRCLADGNYTVKLHFAEI VIRGNKSFHSLGRRIFDVYIQEKLELQDFNIVQAAQGVDKVVVREFKAVVRNKTLDIRFHWAGKGTTAAPEGGTYGPLISAI |
Full Sequence |
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Protein Sequence Length: 1902 Download |
MXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 60 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 120 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 180 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 240 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 300 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 360 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 420 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 480 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 540 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 600 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 660 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 720 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 780 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 840 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXIEFIS LKGQDLASVL PTSLAKLPYL 900 KTIIFSANNL IGELPPSLAN LTKLIEFSVE AQGGQLPRDE EEALEEIAEQ VGKKDWNFSL 960 NPCDGNSNWS TPNRKEMPLY NNTLTCNCSY PNGQCHVVQI FLKGQDLAGV LPSSLEKLPY 1020 LKIIDFTRNY LSGNIPREWA SLQLEYMSLT VNKLSGPIPS FLGNISTLRY MSMESNMFSG 1080 TVPPQLGQLV NLENLILNTN NLTGELPPAL ANLTKLTEFR ISSNNFSGKI PNFIHSWKQL 1140 QKLEIQASGL EGPIPSSISV LTNLTELRIS DLLGEGSNFP PLGNMKGLKK LMLRGCNISG 1200 SIPKYLAEMT ELQILDLSFN KLEGIVPNLE GLTQIEFMYL TSNMLTGSIP DWIESRNNRY 1260 QTDISYNYFS KRSMPSSCRE TLNLFRSFSE RGKLEFDECL DSFPCLKDQY SLHINCGGGR 1320 TIIGDIVYEA DEDLAGPSKF VPTRDNWGFS STGDFWDRDR TTKNYIAHNV SMLGMNDSEL 1380 YTRARLSPLS YTYYGRCLAD GNYTVKLHFA EIVIRGNKSF HSLGRRIFDV YIQEKLELQD 1440 FNIVQAAQGV DKVVVREFKA VVRNKTLDIR FHWAGKGTTA APEGGTYGPL ISAISVKADF 1500 EPPSDGKKKI FIAVGAVAVA LVLFLILGIL WWKVCFGGRI SREQELRGLD LQTGLFTLRQ 1560 IKAATNSFDA ANKIGEGGFG SVYKGTLLDG TIIAVKQLST KSKQGNREFV NEIGMISALQ 1620 HPNLVRLYGC CVEGNQLILV YEYMENNSLA RALFGQVEYQ LNLDWSTRQR ICVGIARGLA 1680 FLHEGSTLKI VHRDIKANNI LLDTNLNPKI SDFGLAKLDE EDNTHISTRV AGTIGYMAPE 1740 YALWGYLTYK ADVYSFGVVA LELVAGKNNM KYRPNEDCFC LLDWAFVLQQ KGNLMELVDP 1800 KLGTEFKKDE AIRMIKVALL CTNPSPALRP TMSAVVSMLK GQTVIQEYPL NPSIYGDEFG 1860 FEALRGQYDQ MQLQSSSDIE PLNHSSHTAQ SGSSLTSSQD P* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00220 | S_TKc | 9.0e-50 | 1572 | 1767 | 198 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
pfam00069 | Pkinase | 3.0e-50 | 1573 | 1767 | 199 | + Protein kinase domain. | ||
cd00192 | PTKc | 3.0e-50 | 1572 | 1840 | 284 | + Catalytic domain of Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers. | ||
cd00180 | PKc | 5.0e-52 | 1574 | 1763 | 194 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
pfam11721 | Malectin | 7.0e-56 | 1310 | 1494 | 188 | + Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan. |
Gene Ontology | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005515 | protein binding |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI30745.1 | 0 | 876 | 1901 | 876 | 1901 | unnamed protein product [Vitis vinifera] |
EMBL | CBI30746.1 | 0 | 924 | 1900 | 22 | 999 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264461.1 | 0.00000000002 | 876 | 1092 | 170 | 386 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264461.1 | 1e-18 | 879 | 1170 | 102 | 367 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264461.1 | 0 | 928 | 1901 | 30 | 1003 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 1552 | 1848 | 16 | 315 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 1552 | 1848 | 16 | 315 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 1552 | 1848 | 24 | 323 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 1552 | 1848 | 24 | 323 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 1552 | 1848 | 24 | 323 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |